Literature summary for 1.3.1.2 extracted from

Van Kuilenburg, A.B.; Meinsma, R.; Beke, E.; Bobba, B.; Boffi, P.; Enns, G.M.; Witt, D.R.; Dobritzsch, D.
Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function (2005), Biol. Chem., 386, 319-324.

Search for more literature for 1.3.1.2

Application

Application	Comment	Organism
medicine	identification of mutations E244V and A551T and splice site mutation IVS11+1G to T in patients with complete loss of enzymic activity	Sus scrofa
medicine	identification of mutations E244V and A551T and splice site mutation IVS11+1G to T in patients with complete loss of enzymic activity	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutants E244V and A551T	Sus scrofa

Protein Variants

Protein Variants	Comment	Organism
A551T	natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation might prevent binding of the prosthetic group FMN and affect folding of the enzyme protein	Sus scrofa
A551T	natural mutation identified in a patient with complete loss of enzymic activity	Homo sapiens
E244V	natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation interferes with the electron flow between NADPH and the pyrimidine binding site of the enzyme	Sus scrofa
E244V	natural mutation identified in a patient with complete loss of enzymic activity	Homo sapiens
additional information	natural mutant IVS11+1G to T leads to a cryptic splice site within exon 11 that results in loss of amino acid residues 400-446 in enzyme primary sequence	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q12882	-	-
Sus scrofa	-	recombinant enzyme	-

Cofactor

Cofactor	Comment	Organism	Structure
FMN	-	Sus scrofa
NADPH	-	Sus scrofa

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Release 2023.1 (January 2023)